2hdn

X-ray diffraction
2.8Å resolution

Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution

Released:
Source organism: Escherichia coli
Primary publication:
Molecular complementarity between tetracycline and the GTPase active site of elongation factor Tu.
Acta Crystallogr D Biol Crystallogr 62 1392-400 (2006)
PMID: 17057344

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-143209 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Elongation factor Tu 1 Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 37 amino acids
Theoretical weight: 3.77 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0CE47 (Residues: 9-45; Coverage: 9%)
Gene names: JW3301, b3339, tufA
Elongation factor Tu 1 Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 335 amino acids
Theoretical weight: 36.97 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0CE47 (Residues: 60-394; Coverage: 85%)
Gene names: JW3301, b3339, tufA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 69.71Å b: 156.06Å c: 134.83Å
α: 90° β: 95.38° γ: 90°
R-values:
R R work R free
0.18 0.18 0.223